Author

Isaak Miller

Date Approved

2022

Degree Type

Open Access Senior Honors Thesis

Department or School

Biology

First Advisor

Brittany Albaugh, Ph.D.

Second Advisor

Hedeel Evans, Ph.D.

Third Advisor

Deborah Heyl-Clegg, Ph.D.

Abstract

Epigenetics is the study of regulating gene expression without changing the DNA sequence. Ubiquitin-like containing Plant Homeodomain and Ring-Finger 2 (UHRF2) is an epigenetic protein that is both overexpressed and underexpressed in various types of cancers. Recent studies have shown the Tandem Tudor Domain (TTD) and Planthomeo Domain (PHD) of UHRF2 interact with histone 3 trimethylated at lysine 9 (H3K9me3). However, the structural basis for UHRF2 TTD-PHD binding H3K9me3 has not been determined. This project consists of purification of the UHRF2 TTD-PHD protein construct expressed in E. coli, crystallization of the protein, X-ray diffraction of the crystal, and molecular replacement and refinement in order to generate the crystal structure of UHRF2 TTD-PHD with H3K9me3. This protein structure will provide critical insights into the molecular mechanism of histone binding by UHRF2, which can eventually be used to specifically target UHRF2 in cancer as a long-term goal.

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